Amylase immobilization on functionalized glass beads by covalent attachment
Yazarlar (4)
M. Vezir Kahraman
Marmara Üniversitesi, Türkiye
Doç. Dr. Gülay BAYRAMOĞLU Marmara Üniversitesi, Türkiye
Nilhan Kayaman-Apohan
Marmara Üniversitesi, Türkiye
Atilla Güngör
Marmara Üniversitesi, Türkiye
Makale Türü Özgün Makale (SSCI, AHCI, SCI, SCI-Exp dergilerinde yayınlanan tam makale)
Dergi Adı Food Chemistry (Q1)
Dergi ISSN 0308-8146 Dergi Bilgileri (2007)
Dergi Tarandığı Indeksler SCI-Expanded
Makale Dili İngilizce Basım Tarihi 01-2007
Kabul Tarihi – Yayınlanma Tarihi 01-01-2007
Cilt / Sayı / Sayfa 104 / 4 / 1385–1392 DOI 10.1016/j.foodchem.2007.01.054
Makale Linki http://linkinghub.elsevier.com/retrieve/pii/S0308814607001562
UAK Araştırma Alanları
Polimer Bilimi
Özet
In this study, α-amylase was covalently immobilized onto phthaloyl chloride-containing amino group functionalized glass beads. In this procedure, amide bonds were formed between amino groups on the protein and acid chloride groups on the glass surface. The surface modified beads were characterized using Fourier transform infrared spectroscopy (FT-IR), scanning electron microscopy (SEM), energy dispersion spectrum (EDS) and UV–Vis spectroscopy. Immobilization was successfully performed under very mild conditions (15°C, 4h). The amount of covalently bound α-amylase was found 25.2±3.1mg/g glass support. The optimum pH value for the free amylase was at pH 6.5. The optimum pH of the immobilized enzyme was shifted 1.0 pH unit to the acidic region. The immobilized α-amylase exhibited better thermostability than the free one. The free enzyme lost all its activity with in 15 days. Covalently bound …
Anahtar Kelimeler
α-Amylase | Covalent immobilization | EDS-SEM | Enzyme | Glass beads
Science Direct
BM Sürdürülebilir Kalkınma Amaçları
Atıf Sayıları
Web of Science 130
Scopus 144
Google Scholar 190
Amylase immobilization on functionalized glass beads by covalent attachment